Skip to main content
SpringerLink
Log in

RuvBL1 and RuvBL2 and Their Complex Proteins Implicated in Many Cellular Pathways

  • Conference paper
  • First Online:
Macromolecular Crystallography

  • 1282 Accesses

Abstract

RuvBL1 and its homolog RuvBL2 belong to the AAA+ family of ATPases and play important roles in chromatin remodeling, in transcriptional regulation, in DNA repair and in the c-Myc and Wnt signaling pathways. Proteins involved in these pathways are often mutated in human cancers. Both RuvBL proteins form a complex and act alone or together in diverse cellular processes. The three-dimensional structures of human RuvBL1 refined using diffraction data to 2.2 Å resolution and of the human RuvBL1/RuvBL2 complex with a truncated domain II at 3 Å resolution are presented. The dodecameric RuvBL1/RuvBL2 complex structure differs from previously described models. It consists of two heterohexameric rings with alternating RuvBL1 and RuvBL2 monomers that interact with each other via domain II. ATPase and helicase activities of RuvBL1 and RuvBL2 were also tested. Interestingly, truncation of domain II resulted not only in a substantial increase of ATP consumption by the RuvBL proteins, but also in stimulation of helicase activity, which was not observed with the full-length proteins.

Sabine Gorynia and Tiago M. Bandeiras contributed equally to this work.

This is a preview of subscription content, log in via an institution to check access.

Access this chapter

Log in via an institution
Chapter
USD 29.95
Price excludes VAT (USA)
  • Available as PDF
  • Read on any device
  • Instant download
  • Own it forever
eBook
USD 129.00
Price excludes VAT (USA)
  • Available as EPUB and PDF
  • Read on any device
  • Instant download
  • Own it forever
Softcover Book
USD 169.99
Price excludes VAT (USA)
  • Compact, lightweight edition
  • Dispatched in 3 to 5 business days
  • Free shipping worldwide - see info
Hardcover Book
USD 169.99
Price excludes VAT (USA)
  • Durable hardcover edition
  • Dispatched in 3 to 5 business days
  • Free shipping worldwide - see info

Tax calculation will be finalised at checkout

Purchases are for personal use only

Institutional subscriptions

References

  1. Bauer A, Huber O, Kemler R (1998) Pontin52, an interaction partner of beta-catenin, binds to the TATA box binding protein. Proc Natl Acad Sci USA 95(25):14787–14792

    Article  ADS  Google Scholar 

  2. Neuwald AF et al (1999) AAA+: a class of chaperone-like ATPases associated with the assembly, operation, and disassembly of protein complexes. Genome Res 9(1):27–43

    Google Scholar 

  3. Walker JE et al (1982) Distantly related sequences in the alpha- and beta-subunits of ATP synthase, myosin, kinases and other ATP-requiring enzymes and a common nucleotide binding fold. EMBO J 1(8):945–951

    Google Scholar 

  4. Feng Y, Lee N, Fearon ER (2003) TIP49 regulates beta-catenin-mediated neoplastic transformation and T-cell factor target gene induction via effects on chromatin remodeling. Cancer Res 63(24):8726–8734

    Google Scholar 

  5. Jonsson ZO et al (2004) Rvb1p/Rvb2p recruit Arp5p and assemble a functional Ino80 chromatin remodeling complex. Mol Cell 16(3):465–477

    Article  Google Scholar 

  6. Wood MA, McMahon SB, Cole MD (2000) An ATPase/helicase complex is an essential cofactor for oncogenic transformation by c-Myc. Mol Cell 5(2):321–330

    Article  Google Scholar 

  7. Putnam CD et al (2001) Structure and mechanism of the RuvB Holliday junction branch migration motor. J Mol Biol 311(2):297–310

    Article  MathSciNet  Google Scholar 

  8. Yamada K et al (2001) Crystal structure of the Holliday junction migration motor protein RuvB from Thermus thermophilus HB8. Proc Natl Acad Sci USA 98(4):1442–1447

    Article  ADS  Google Scholar 

  9. Tsaneva IR, Muller B, West SC (1993) RuvA and RuvB proteins of Escherichia coli exhibit DNA helicase activity in vitro. Proc Natl Acad Sci USA 90(4):1315–1319

    Article  ADS  Google Scholar 

  10. Mezard C et al (1999) Escherichia coli RuvBL268S: a mutant RuvB protein that exhibits wild-type activities in vitro but confers a UV-sensitive ruv phenotype in vivo. Nucleic Acids Res 27(5):1275–1282

    Article  Google Scholar 

  11. Ikura T et al (2000) Involvement of the TIP60 histone acetylase complex in DNA repair and apoptosis. Cell 102(4):463–473

    Article  Google Scholar 

  12. Fuchs M et al (2001) The p400 complex is an essential E1A transformation target. Cell 106(3):297–307

    Article  Google Scholar 

  13. Samuelson AV et al (2005) p400 is required for E1A to promote apoptosis. J Biol Chem 280(23):21915–21923

    Article  Google Scholar 

  14. Jin J et al (2005) In and out: histone variant exchange in chromatin. Trends Biochem Sci 30(12):680–687

    Article  Google Scholar 

  15. Jonsson ZO et al (2001) Rvb1p and Rvb2p are essential components of a chromatin remodeling complex that regulates transcription of over 5% of yeast genes. J Biol Chem 276(19):16279–16288

    Article  Google Scholar 

  16. Shen X et al (2000) A chromatin remodelling complex involved in transcription and DNA processing. Nature 406(6795):541–544

    Article  ADS  Google Scholar 

  17. Kanemaki M et al (1997) Molecular cloning of a rat 49-kDa TBP-interacting protein (TIP49) that is highly homologous to the bacterial RuvB. Biochem Biophys Res Commun 235(1):64–68

    Article  Google Scholar 

  18. Kanemaki M et al (1999) TIP49b, a new RuvB-like DNA helicase, is included in a complex together with another RuvB-like DNA helicase, TIP49a. J Biol Chem 274(32):22437–22444

    Article  Google Scholar 

  19. Qiu XB et al (1998) An eukaryotic RuvB-like protein (RUVBL1) essential for growth. J Biol Chem 273(43):27786–27793

    Article  Google Scholar 

  20. Bauer A et al (2000) Pontin52 and reptin52 function as antagonistic regulators of beta-catenin signalling activity. EMBO J 19(22):6121–6130

    Article  Google Scholar 

  21. Dugan KA, Wood MA, Cole MD (2002) TIP49, but not TRRAP, modulates c-Myc and E2F1 dependent apoptosis. Oncogene 21(38):5835–5843

    Article  Google Scholar 

  22. Cho SG et al (2001) TIP49b, a regulator of activating transcription factor 2 response to stress and DNA damage. Mol Cell Biol 21(24):8398–8413

    Article  Google Scholar 

  23. Cole MD (1986) The myc oncogene: its role in transformation and differentiation. Annu Rev Genet 20:361–384

    Article  Google Scholar 

  24. Evan GI et al (1992) Induction of apoptosis in fibroblasts by c-myc protein. Cell 69(1):119–128

    Article  Google Scholar 

  25. Li LH et al (1994) c-Myc represses transcription in vivo by a novel mechanism dependent on the initiator element and Myc box II. EMBO J 13(17):4070–4079

    Google Scholar 

  26. Penn LJ et al (1990) Negative autoregulation of c-myc transcription. EMBO J 9(4):1113–1121

    MathSciNet  Google Scholar 

  27. Stone J et al (1987) Definition of regions in human c-myc that are involved in transformation and nuclear localization. Mol Cell Biol 7(5):1697–1709

    ADS  Google Scholar 

  28. Matias PM et al (2006) Crystal structure of the human AAA+ protein RuvBL1. J Biol Chem 281(50):38918–38929

    Article  Google Scholar 

  29. Gorynia S et al (2008) Cloning, expression, purification, crystallization and preliminary X-ray analysis of the human RuvBL1-RuvBL2 complex. Acta Crystallogr Sect F Struct Biol Cryst Commun 64(Pt 9):840–846

    Article  Google Scholar 

  30. Gorynia S et al (2010) Structural and functional insights into the dodecameric molecular machine – The RuvBL1/RuvBL2 complex. J Struct Biol 176 (2011), 279–291

    Google Scholar 

  31. Puri T et al (2007) Dodecameric structure and ATPase activity of the human TIP48/TIP49 complex. J Mol Biol 366(1):179–192

    Article  Google Scholar 

  32. Torreira E et al (2008) Architecture of the pontin/reptin complex, essential in the assembly of several macromolecular complexes. Structure 16(10):1511–1520

    Article  Google Scholar 

  33. Gribun A et al (2008) Yeast Rvb1 and Rvb2 are ATP-dependent DNA helicases that form a heterohexameric complex. J Mol Biol 376(5):1320–1333

    Article  Google Scholar 

  34. Diop SB et al (2008) Reptin and pontin function antagonistically with PcG and TrxG complexes to mediate Hox gene control. EMBO Rep 9(3):260–266

    Article  MathSciNet  Google Scholar 

Download references

Author information

Authors and Affiliations

  1. Instituto de Tecnologia Química e Biológica, Universidade Nova de Lisboa, Apartado 127, 2781-901, Oeiras, Portugal

    Sabine Gorynia, Pedro M. Matias, Colin E. McVey, Peter Donner & Maria Arménia Carrondo

  2. Lead Discovery Berlin – Protein Supply, Bayer Schering Pharma AG, 13353, Berlin, Germany

    Sabine Gorynia

  3. Department of Biological Chemistry, David Geffen School of Medicine, UCLA, 615 Charles E. Young Drive South, 951737, Los Angeles, CA, 90095-1737, USA

    Sabine Gorynia

  4. Instituto de Biologia Experimental e Tecnológica, Apartado 12, 2781-901, Oeiras, Portugal

    Tiago M. Bandeiras & Filipa G. Pinho

Authors
  1. Sabine Gorynia
    View author publications

    You can also search for this author in PubMed Google Scholar

  2. Tiago M. Bandeiras
    View author publications

    You can also search for this author in PubMed Google Scholar

  3. Pedro M. Matias
    View author publications

    You can also search for this author in PubMed Google Scholar

  4. Filipa G. Pinho
    View author publications

    You can also search for this author in PubMed Google Scholar

  5. Colin E. McVey
    View author publications

    You can also search for this author in PubMed Google Scholar

  6. Peter Donner
    View author publications

    You can also search for this author in PubMed Google Scholar

  7. Maria Arménia Carrondo
    View author publications

    You can also search for this author in PubMed Google Scholar

Corresponding author

Correspondence to Maria Arménia Carrondo .

Editor information

Editors and Affiliations

  1. , Instit.de Technologia Química e Biológia, Universidade Nova de Lisboa, Rua da Quinta Grande , Apartado 127 6, Oeiras, 2781-901, Portugal

    Maria Armenia Carrondo

  2. Dipto. Scienze Chimiche, Università di Padova, Via F. Marzolo 1, Padova, 35131, Italy

    Paola Spadon

Rights and permissions

Reprints and permissions

Copyright information

© 2012 Springer Science+Business Media B.V.

About this paper

Cite this paper

Gorynia, S. et al. (2012). RuvBL1 and RuvBL2 and Their Complex Proteins Implicated in Many Cellular Pathways. In: Carrondo, M., Spadon, P. (eds) Macromolecular Crystallography. NATO Science for Peace and Security Series A: Chemistry and Biology. Springer, Dordrecht. https://doi.org/10.1007/978-94-007-2530-0_5

Download citation

Publish with us

Policies and ethics

Search

Navigation